A5063155873- Heat shock proteins research
- Protein Structure and Dynamics
- Advanced Fluorescence Microscopy Techniques
- ATP Synthase and ATPases Research
- Genomics and Chromatin Dynamics
- RNA Research and Splicing
- Prenatal Screening and Diagnostics
- Microbial Inactivation Methods
- Chromosomal and Genetic Variations
- Molecular Junctions and Nanostructures
- Simulation Techniques and Applications
- Advanced Electron Microscopy Techniques and Applications
- DNA and Nucleic Acid Chemistry
- Advanced biosensing and bioanalysis techniques
- Scientific Computing and Data Management
- Advanced Clustering Algorithms Research
- thermodynamics and calorimetric analyses
- Listeria monocytogenes in Food Safety
- Retinal Development and Disorders
- Single-cell and spatial transcriptomics
- Cancer Genomics and Diagnostics
- Machine Learning in Materials Science
- Plant Molecular Biology Research
- Advanced Biosensing Techniques and Applications
- Veterinary medicine and infectious diseases
PicoQuant (Germany)
2021-2024
Centre de Biologie Structurale
2018-2024
Inserm
2020-2022
Université de Montpellier
2020-2022
Centre National de la Recherche Scientifique
2018-2022
University of Freiburg
2016-2018
Center for Integrated Protein Science Munich
2011
Technical University of Munich
2011
University of Würzburg
1997-1998
Single-molecule Förster resonance energy transfer (smFRET) is increasingly being used to determine distances, structures, and dynamics of biomolecules in vitro vivo. However, generalized protocols FRET standards ensure the reproducibility accuracy measurements efficiencies are currently lacking. Here we report results a comparative blind study which 20 labs determined (E) several dye-labeled DNA duplexes. Using unified, straightforward method, obtained with s.d. between ±0.02 ±0.05. We...
Abstract Single-molecule FRET (smFRET) is a versatile technique to study the dynamics and function of biomolecules since it makes nanoscale movements detectable as fluorescence signals. The powerful ability infer quantitative kinetic information from smFRET data is, however, complicated by experimental limitations. Diverse analysis tools have been developed overcome these hurdles but systematic comparison lacking. Here, we report results blind benchmark assessing eleven used rate constants...
We use plasmon rulers to follow the conformational dynamics of a single protein for up 24 h at video rate. The ruler consists two gold nanospheres connected by linker. In our experiment, we molecular chaperone heat shock 90 (Hsp90), which is known show "open" and "closed" conformations. Our measurements confirm previously with transition times in second minute time scale reveals new on minutes hours. Plasmon thus extend observation bandwidth 3–4 orders magnitude respect single-molecule...
Abstract Genome-wide ensemble sequencing methods improved our understanding of chromatin organization in eukaryotes but lack the ability to capture single-cell heterogeneity and spatial organization. To overcome these limitations, new imaging-based have emerged, giving rise field genomics. Here, we present pyHiM, a user-friendly python toolbox specifically designed for analysis multiplexed DNA-FISH data reconstruction traces individual cells. pyHiM employs modular architecture, allowing...
Abstract The spatial organization of chromatin at the scale topologically associating domains (TADs) and below displays large cell-to-cell variations. Up until now, how this heterogeneity in conformation is shaped by condensation, TAD insulation, transcription has remained mostly elusive. Here, we used Hi-M, a multiplexed DNA-FISH imaging technique providing developmental timing transcriptional status, to show that emergence TADs ensemble level partially segregates conformational space...
The molecular chaperone and heat-shock protein Hsp90 has become a central target in anti-cancer therapy. Nevertheless, the effect of inhibition is still not understood at level, preventing truly rational drug design. Here we report on most prominent candidates, namely, radicicol, geldanamycin, derivatives purine, novobiocin, Hsp90's characteristic conformational dynamics binding three interaction partners. Unexpectedly, global opening closing transitions are hardly affected by inhibitors....
Single-molecule Förster resonance energy transfer (smFRET) has become a widely used biophysical technique to study the dynamics of biomolecules.For many molecular machines in cell proteins have act together with interaction partners functional cycle fulfill their task.The extension two-color multi-color smFRET makes it possible simultaneously probe more than one or conformational change.This not only adds new dimension experiments but also offers unique possibility directly sequence events...
This paper was originally published under standard Springer Nature copyright. As of the date this correction, Analysis is available online as an open-access with a CC-BY license. No other part has been changed.
Abstract During development, naïve cells gradually acquire distinct cell fates, through sophisticated mechanisms of precise spatio-temporal gene regulation. Acquisition fate is thought to rely on the specific interaction remote cis -regulatory modules (e.g. enhancers, silencers) (CRM) and target promoters. However, interplay between chromatin structure expression still unclear, particularly in single within multicellular developing organisms. Here we employ Hi-M, a single-cell spatial...
ABSTRACT Single-molecule FRET (smFRET) is a versatile technique to study the dynamics and function of biomolecules since it makes nanoscale movements detectable as fluorescence signals. The powerful ability infer quantitative kinetic information from smFRET data is, however, complicated by experimental limitations. Diverse analysis tools have been developed overcome these hurdles but systematic comparison lacking. Here, we report results blind benchmark assessing eleven used rate constants...
We present a simple and robust technique to extract kinetic rate models thermodynamic quantities from single molecule time traces. SMACKS (Single Molecule Analysis of Complex Kinetic Sequences) is maximum likelihood approach that works equally well for long trajectories as set short ones. It resolves all statistically relevant rates also their uncertainties. This achieved by optimizing one global model based on the complete dataset, while allowing experimental variations between individual...
Abstract The molecular chaperone and heat-shock protein Hsp90 has become a central target in anti-cancer therapy. Nevertheless, the effect of inhibition is still not understood at level, preventing truly rational drug design. Here we report on most prominent candidates, namely radicicol, geldanamycin, derivatives purine novobiocin, Hsp90’s characteristic conformational dynamics binding three interaction partners. Unexpectedly, global opening closing transitions are hardly affected by...